Introduction

The mammalian proteome has been estimated to contain multiple millions of unique proteoforms. This level of complexity is derived from a relatively simple genome (approx. 25,000 genes), a transcriptome which increases the potential protein footprint to 100,000, and protein post-translational modifications (PTMs) which account for the vast increase in proteome complexity and an almost limitless potential for functional diversity. This information suggests that nearly all proteins will be modified by multiple PTMs. For any given protein, a variety of PTM proteoforms offer a way to facilitate rapid cellular changes by altering the structure and function of the protein. 

In many cases PTMs have been shown to work in concert to orchestrate a specific protein function and recent studies have suggested that both cooperative and negative PTM crosstalk is a pervasive and fundamental cell regulatory mechanism.

Importantly for human health and disease, misregulation of PTMs has been implicated in the progression of diseases like cancer, heart failure, neurologic, and metabolic diseases.

See the table below for information about key, regulatory protein modifications, or go to ModPred (also found in our resources link) to see if your target protein may potentially be modified.